LIVIVO - Search results -

Search results

Result 1 - 10 of total 101

Search options

Article ; Online: Macroautophagy: a mechanism for mediating cell death or for promoting cell survival?

Lieberthal, Wilfred

2008 Volume 74, Issue 5, Page(s) 555–557

Abstract: Macroautophagy is a ubiquitous mechanism for the bulk removal of macromolecules and cell organelles from the cell. Periyasamy-Thandavan and colleagues report that cisplatin activates autophagy in renal tubular cells and that autophagy plays a role in ... ...

Abstract	Macroautophagy is a ubiquitous mechanism for the bulk removal of macromolecules and cell organelles from the cell. Periyasamy-Thandavan and colleagues report that cisplatin activates autophagy in renal tubular cells and that autophagy plays a role in decreasing apoptosis of tubular cells induced by cisplatin. This finding provides novel evidence that autophagy may play a role in ameliorating the effects of acute injury on the kidney.
MeSH term(s)	Animals ; Antineoplastic Agents/toxicity ; Autophagy/drug effects ; Autophagy/physiology ; Cell Death/physiology ; Cell Survival/physiology ; Cisplatin/toxicity ; Humans ; Kidney/injuries ; Kidney/pathology ; Kidney Tubules/drug effects ; Kidney Tubules/pathology ; Kidney Tubules/physiopathology
Chemical Substances	Antineoplastic Agents ; Cisplatin (Q20Q21Q62J)
Language	English
Publishing date	2008-09
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	120573-0
ISSN	1523-1755 ; 0085-2538
ISSN (online)	1523-1755
ISSN	0085-2538
DOI	10.1038/ki.2008.325
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 797: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Poly(ethylene glycol)-containing hydrogels modulate α-defensin release from polymorphonuclear leukocytes and monocyte recruitment.

Lieberthal, Tyler Jacob / Cohen, Hannah Caitlin / Kao, W John

Journal of biomedical materials research. Part A

2015 Volume 103, Issue 12, Page(s) 3772–3780

Abstract: Polymorphonuclear leukocytes (PMNs) release granule proteins as the first line of defense against bacteria and set up chemotactic gradients that result in monocyte infiltration to the site of injury. Although well established, the role of biomaterials in ...

Abstract	Polymorphonuclear leukocytes (PMNs) release granule proteins as the first line of defense against bacteria and set up chemotactic gradients that result in monocyte infiltration to the site of injury. Although well established, the role of biomaterials in regulating adherent PMN degranulation and subsequent PMN-monocyte paracrine interactions is less clear. The aim of this study was to determine how biomaterials affect the degranulation of selected biomarkers and downstream monocyte adhesion and transendothelial migration. Poly(ethylene glycol) (PEG)-containing hydrogels (PEG and an interpenetrating network of PEG and gelatin) promote the release of the α-defensins human neutrophil peptides 1-3, but not azurocidin or monocyte chemotactic protein-1. Although human neutrophil peptides 1-3 are monocyte chemoattractants, no subsequent effects on monocyte transmigration are observed in static conditions. Under flow conditions, monocyte adhesion on human umbilical vein endothelial cells stimulated with tumor necrosis factor-α is elevated in the presence of granule proteins from PMNs adherent on polydimethylsiloxane, but not from PMNs cultured on PEG hydrogels. These results suggest that PEG promotes PMN antimicrobial capacity without enhanced monocyte recruitment.
MeSH term(s)	Biocompatible Materials/metabolism ; Cell Adhesion ; Cell Degranulation ; Cells, Cultured ; Chemotaxis, Leukocyte ; Human Umbilical Vein Endothelial Cells ; Humans ; Hydrogels/metabolism ; Monocytes/cytology ; Monocytes/metabolism ; Neutrophils/cytology ; Neutrophils/metabolism ; Polyethylene Glycols/metabolism ; alpha-Defensins/metabolism
Chemical Substances	Biocompatible Materials ; Hydrogels ; alpha-Defensins ; Polyethylene Glycols (30IQX730WE)
Language	English
Publishing date	2015-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	2099989-6
ISSN	1552-4965 ; 1549-3296 ; 0021-9304
ISSN (online)	1552-4965
ISSN	1549-3296 ; 0021-9304
DOI	10.1002/jbm.a.35519
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 6195: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: AMPK-mediated activation of Akt protects renal tubular cells from stress-induced apoptosis in vitro and ameliorates ischemic AKI in vivo.

Lieberthal, Wilfred / Tang, Meiyi / Abate, Mersema / Lusco, Mark / Levine, Jerrold S

American journal of physiology. Renal physiology

2019 Volume 317, Issue 7, Page(s) F1–F11

Abstract: We have reported that preconditioning renal tubular cells (RTCs) with A-769662 [a pharmacological activator of AMP-activated protein kinase (AMPK)] reduces apoptosis of RTCs induced by subsequent stress and ameliorates the severity of ischemic acute ... ...

Abstract	We have reported that preconditioning renal tubular cells (RTCs) with A-769662 [a pharmacological activator of AMP-activated protein kinase (AMPK)] reduces apoptosis of RTCs induced by subsequent stress and ameliorates the severity of ischemic acute kidney injury (AKI) in mice. In the present study, we examined the role of the phosphoinositide 3-kinase (PI3K)/Akt pathway in mediating these effects. Using shRNA, we developed knockdown (KD) RTCs to confirm that any novel effects of A-769662 are mediated specifically by AMPK. We reduced expression of the total β-domain of AMPK in KD RTCs by >80%. Control RTCs were transfected with "scrambled" shRNA. Preconditioning control RTCs with A-769662 increased both the phosphorylation (activity) of AMPK and survival of these cells when exposed to subsequent stress, but neither effect was observed in KD cells. These data demonstrate that activation of AMPK by A-769662 is profoundly impaired in KD cells. A-769662 activated PI3K and Akt in control but not KD RTCs. These data provide novel evidence that activation of the PI3K/Akt pathway by A-769662 is mediated specifically through activation of AMPK and not by a nonspecific mechanism. We also demonstrate that, in control RTCs, Akt plays a role in mediating the antiapoptotic effects of A-769662. In addition, we provide evidence that AMPK ameliorates the severity of ischemic AKI in mice and that this effect is also partially mediated by Akt. Finally, we provide evidence that AMPK activates PI3K by inhibiting mechanistic target of rapamycin complex 1 and preventing mechanistic target of rapamycin complex 1-mediated inhibition of insulin receptor substrate-1-associated activation of PI3K.
MeSH term(s)	AMP-Activated Protein Kinases/genetics ; AMP-Activated Protein Kinases/physiology ; Acute Kidney Injury/etiology ; Acute Kidney Injury/pathology ; Acute Kidney Injury/prevention & control ; Animals ; Apoptosis/drug effects ; Apoptosis/physiology ; Cell Line ; Enzyme Activation/drug effects ; Gene Knockdown Techniques ; Insulin Receptor Substrate Proteins/physiology ; Ischemic Preconditioning ; Kidney/blood supply ; Kidney Tubules, Proximal/drug effects ; Kidney Tubules, Proximal/pathology ; Mechanistic Target of Rapamycin Complex 1/antagonists & inhibitors ; Mice ; Phosphatidylinositol 3-Kinase/metabolism ; Proto-Oncogene Proteins c-akt/physiology ; Pyrones/pharmacology ; Reperfusion Injury/complications ; Thiophenes/pharmacology
Chemical Substances	Insulin Receptor Substrate Proteins ; Pyrones ; Thiophenes ; Phosphatidylinositol 3-Kinase (EC 2.7.1.137) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; AMP-Activated Protein Kinases (EC 2.7.11.31) ; 4-hydroxy-3-(4-(2-hydroxyphenyl)phenyl)-6-oxo-7H-thieno(2,3-b)pyridine-5-carbonitrile (P68477CD2C)
Language	English
Publishing date	2019-04-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	603837-2
ISSN	1522-1466 ; 0363-6127
ISSN (online)	1522-1466
ISSN	0363-6127
DOI	10.1152/ajprenal.00553.2018
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.89: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Mammalian target of rapamycin and the kidney. II. Pathophysiology and therapeutic implications.

Lieberthal, Wilfred / Levine, Jerrold S

American journal of physiology. Renal physiology

2012 Volume 303, Issue 2, Page(s) F180–91

Abstract: The mTOR pathway plays an important role in a number of common renal diseases, including acute kidney injury (AKI), diabetic nephropathy (DN), and polycystic kidney diseases (PKD). The activity of mTOR complex 1 (mTORC1) is necessary for renal ... ...

Abstract	The mTOR pathway plays an important role in a number of common renal diseases, including acute kidney injury (AKI), diabetic nephropathy (DN), and polycystic kidney diseases (PKD). The activity of mTOR complex 1 (mTORC1) is necessary for renal regeneration and repair after AKI, and inhibition of mTORC1 by rapamycin has been shown to delay recovery from ischemic AKI in animal studies, and to prolong delayed graft function in humans who have received a kidney transplant. For this reason, administration of rapamycin should be delayed or discontinued in patients with AKI until full recovery of renal function has occurred. On the other hand, inappropriately high mTORC1 activity contributes to the progression of the metabolic syndrome, the development of type 2 diabetes, and the pathogenesis of DN. In addition, chronic hyperactivity of mTORC1, and possibly also mTORC2, contributes to cyst formation and enlargement in a number of forms of PKD. Inhibition of mTOR, using either rapamycin (which inhibits predominantly mTORC1) or "catalytic" inhibitors (which effectively inhibit both mTORC1 and mTORC2), provide exciting possibilities for novel forms of treatment of DN and PKD. In this second part of the review, we will examine the role of mTOR in the pathophysiology of DN and PKD, as well as the potential utility of currently available and newly developed inhibitors of mTOR to slow the progression of DN and/or PKD.
MeSH term(s)	Acute Kidney Injury/physiopathology ; Acute Kidney Injury/therapy ; Diabetic Nephropathies/drug therapy ; Diabetic Nephropathies/physiopathology ; Humans ; Kidney/physiopathology ; Mechanistic Target of Rapamycin Complex 1 ; Multiprotein Complexes ; Polycystic Kidney Diseases/drug therapy ; Polycystic Kidney Diseases/physiopathology ; Proteins/physiology ; Sirolimus/therapeutic use ; TOR Serine-Threonine Kinases/physiology ; Transcription Factors/physiology
Chemical Substances	CRTC2 protein, human ; Multiprotein Complexes ; Proteins ; Transcription Factors ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Sirolimus (W36ZG6FT64)
Language	English
Publishing date	2012-07-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	603837-2
ISSN	1522-1466 ; 0363-6127
ISSN (online)	1522-1466
ISSN	0363-6127
DOI	10.1152/ajprenal.00015.2012
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.89: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Mammalian target of rapamycin and the kidney. I. The signaling pathway.

Lieberthal, Wilfred / Levine, Jerrold S

American journal of physiology. Renal physiology

2012 Volume 303, Issue 1, Page(s) F1–10

Abstract: The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that plays a fundamental role in regulating cellular homeostasis and metabolism. In a two-part review, we examine the complex molecular events involved in the regulation and downstream ...

Abstract	The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that plays a fundamental role in regulating cellular homeostasis and metabolism. In a two-part review, we examine the complex molecular events involved in the regulation and downstream effects of mTOR, as well as the pivotal role played by this kinase in many renal diseases, particularly acute kidney injury, diabetic nephropathy, and polycystic kidney diseases. Here, in the first part of the review, we provide an overview of the complex signaling events and pathways governing mTOR activity and action. mTOR is a key component of two multiprotein complexes, known as mTOR complex 1 (mTORC1) and 2 (mTORC2). Some proteins are found in both mTORC1 and mTORC2, while others are unique to one or the other complex. Activation of mTORC1 promotes cell growth (increased cellular mass or size) and cell proliferation (increased cell number). mTORC1 acts as a metabolic "sensor," ensuring that conditions are optimal for both cell growth and proliferation. Its activity is tightly regulated by the availability of amino acids, growth factors, energy stores, and oxygen. The effects of mTORC2 activation are distinct from those of mTORC1. Cellular processes modulated by mTORC2 include cell survival, cell polarity, cytoskeletal organization, and activity of the aldosterone-sensitive sodium channel. Upstream events controlling mTORC2 activity are less well understood than those controlling mTORC1, although growth factors appear to stimulate both complexes. Rapamycin and its analogs inhibit the activity of mTORC1 only, and not that of mTORC2, while the newer "catalytic" mTOR inhibitors affect both complexes.
MeSH term(s)	Animals ; Cell Proliferation ; Humans ; Kidney/metabolism ; Kidney Diseases/metabolism ; Phosphorylation ; Signal Transduction/physiology ; TOR Serine-Threonine Kinases/metabolism
Chemical Substances	TOR Serine-Threonine Kinases (EC 2.7.1.1)
Language	English
Publishing date	2012-07-01
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	603837-2
ISSN	1522-1466 ; 0363-6127
ISSN (online)	1522-1466
ISSN	0363-6127
DOI	10.1152/ajprenal.00014.2012
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.89: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Talin: a mechanosensitive molecule in health and disease.

Haining, Alexander W M / Lieberthal, Tyler J / Del Río Hernández, Armando

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2016 Volume 30, Issue 6, Page(s) 2073–2085

Abstract: ... its relationship to binding partners, and its role in disease states.-Haining, A. W. M., Lieberthal, T. J., del Río ...

Abstract	Talin is a ubiquitous, large focal adhesion protein that links intracellular networks with the extracellular matrix (ECM) via its connection with the actin cytoskeleton and membrane integrins. It is one of a handful molecules that can expose new recognition sites when undergoing force-induced mechanical unfolding, and it can bind and recruit cytoskeletal proteins that are involved in mechanotransduction. Talin has attracted great interest in the field of mechanobiology because of its plasticity in undergoing conformational changes under force stimulation as well as its cellular localization that bridges the cytoskeleton with the ECM. In addition to these roles in healthy cells, the dysregulation of talin activators can lead to disease states in which aberrant integrin activation and mechanotransduction precipitate changes in cell spreading, migration, and survival. New data have implicated a role for talin in diseases that are highly regulated by mechanical cues. In this review, we present the current understanding of talin structure, its relationship to binding partners, and its role in disease states.-Haining, A. W. M., Lieberthal, T. J., del Río Hernández, A. Talin: a mechanosensitive molecule in health and disease.
MeSH term(s)	Animals ; Cytoskeleton/physiology ; Gene Expression Regulation/physiology ; Hematologic Diseases/metabolism ; Mechanotransduction, Cellular/physiology ; Neoplasms/genetics ; Neoplasms/metabolism ; Neoplasms/therapy ; Protein Binding ; Talin/chemistry ; Talin/genetics ; Talin/metabolism
Chemical Substances	Talin
Language	English
Publishing date	2016
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.201500080R
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 2266: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 296: Show issues

Order via subito

Details ▾

Article ; Online: Poly(ethylene glycol)-containing hydrogels promote the release of primary granules from human blood-derived polymorphonuclear leukocytes.

Cohen, Hannah Caitlin / Lieberthal, Tyler Jacob / Kao, W John

Journal of biomedical materials research. Part A

2014 Volume 102, Issue 12, Page(s) 4252–4261

Abstract: Polymorphonuclear leukocytes (PMNs) are recruited to sites of injury and biomaterial implants. Once activated, PMNs can exocytose their granule subsets to recruit monocytes (MCs) and mediate MC/macrophage activation. We investigated the release of ... ...

Abstract	Polymorphonuclear leukocytes (PMNs) are recruited to sites of injury and biomaterial implants. Once activated, PMNs can exocytose their granule subsets to recruit monocytes (MCs) and mediate MC/macrophage activation. We investigated the release of myeloperoxidase (MPO), a primary granule marker, and matrix metalloproteinase-9 (MMP-9), a tertiary granule marker, from human blood-derived PMNs cultured on poly(ethylene glycol) (PEG) hydrogels, polydimethylsiloxane (PDMS), tissue culture polystyrene (TCPS) and gelatin-PEG (GP) hydrogels, with and without the presence of the bacterial peptide formyl-Met-Leu-Phe. Supernatants from PMN cultures on PEG-containing hydrogels (i.e., PEG and GP hydrogels) had higher concentrations of MPO than those from PMN cultures on PDMS or TCPS at 2 h. PMNs on all biomaterials released comparable levels of MMP-9 at 2 h, indicating that PMNs cultured on PEG-containing hydrogels have different mechanisms of release for primary and tertiary granules. Src family kinases were involved in the release of MPO from PMNs cultured on PEG hydrogels, TCPS and GP hydrogels and in the release of MMP-9 from PMNs cultured on all four biomaterials. The increased release of primary granules from PMNs on PEG-containing hydrogels did not significantly increase MC chemotaxis, indicating that additional co-effectors in the dynamic inflammatory milieu in vivo modulate PMN-mediated MC recruitment.
MeSH term(s)	Chemotaxis ; Culture Media, Conditioned/chemistry ; Humans ; Hydrogels/chemistry ; Macrophage Activation/drug effects ; Macrophages/cytology ; Macrophages/metabolism ; Matrix Metalloproteinase 9/chemistry ; Monocytes/cytology ; Monocytes/metabolism ; N-Formylmethionine Leucyl-Phenylalanine/pharmacology ; Neutrophils/cytology ; Neutrophils/metabolism ; Polyethylene Glycols/chemistry ; Secretory Vesicles/chemistry
Chemical Substances	Culture Media, Conditioned ; Hydrogels ; Polyethylene Glycols (3WJQ0SDW1A) ; N-Formylmethionine Leucyl-Phenylalanine (59880-97-6) ; MMP9 protein, human (EC 3.4.24.35) ; Matrix Metalloproteinase 9 (EC 3.4.24.35)
Language	English
Publishing date	2014-02-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2099989-6
ISSN	1552-4965 ; 1549-3296 ; 0021-9304
ISSN (online)	1552-4965
ISSN	1549-3296 ; 0021-9304
DOI	10.1002/jbm.a.35101
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 6195: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article: Navigating the Collagen Jungle: The Biomedical Potential of Fiber Organization in Cancer.

Ouellette, Jonathan N / Drifka, Cole R / Pointer, Kelli B / Liu, Yuming / Lieberthal, Tyler J / Kao, W John / Kuo, John S / Loeffler, Agnes G / Eliceiri, Kevin W

Bioengineering (Basel, Switzerland)

2021 Volume 8, Issue 2

Abstract: Recent research has highlighted the importance of key tumor microenvironment features, notably the collagen-rich extracellular matrix (ECM) in characterizing tumor invasion and progression. This led to great interest from both basic researchers and ... ...

Abstract	Recent research has highlighted the importance of key tumor microenvironment features, notably the collagen-rich extracellular matrix (ECM) in characterizing tumor invasion and progression. This led to great interest from both basic researchers and clinicians, including pathologists, to include collagen fiber evaluation as part of the investigation of cancer development and progression. Fibrillar collagen is the most abundant in the normal extracellular matrix, and was revealed to be upregulated in many cancers. Recent studies suggested an emerging theme across multiple cancer types in which specific collagen fiber organization patterns differ between benign and malignant tissue and also appear to be associated with disease stage, prognosis, treatment response, and other clinical features. There is great potential for developing image-based collagen fiber biomarkers for clinical applications, but its adoption in standard clinical practice is dependent on further translational and clinical evaluations. Here, we offer a comprehensive review of the current literature of fibrillar collagen structure and organization as a candidate cancer biomarker, and new perspectives on the challenges and next steps for researchers and clinicians seeking to exploit this information in biomedical research and clinical workflows.
Language	English
Publishing date	2021-01-21
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2746191-9
ISSN	2306-5354
ISSN	2306-5354
DOI	10.3390/bioengineering8020017
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Biology of ischemic and toxic renal tubular cell injury: role of nitric oxide and the inflammatory response.

Lieberthal, W

Current opinion in nephrology and hypertension

1998 Volume 7, Issue 3, Page(s) 289–295

Abstract: Acute ischemic or toxic injury to the kidney induces alterations in the expression of many genes. Some of these molecular responses have been termed 'maladaptive' because they exacerbate the tubular damage induced by the initiating insult. Some ... ...

Abstract	Acute ischemic or toxic injury to the kidney induces alterations in the expression of many genes. Some of these molecular responses have been termed 'maladaptive' because they exacerbate the tubular damage induced by the initiating insult. Some maladaptive responses include alterations in the activity of nitric oxide synthases and expression of cytokines and adhesion molecules that mediate an inflammatory response. This review focuses on the role of nitric oxide and inflammation in influencing the course of acute renal failure due to ischemic and toxic tubular injury.
MeSH term(s)	Acute Kidney Injury/drug therapy ; Acute Kidney Injury/etiology ; Acute Kidney Injury/physiopathology ; Animals ; Humans ; Inflammation/etiology ; Inflammation/physiopathology ; Ischemia/physiopathology ; Kidney Tubules/blood supply ; Kidney Tubules/injuries ; Kidney Tubules/physiopathology ; Leukocytes/physiology ; Nitric Oxide/physiology ; Nitric Oxide Synthase/physiology ; Nitric Oxide Synthase Type II ; Nitric Oxide Synthase Type III ; T-Lymphocytes/physiology ; alpha-MSH/therapeutic use
Chemical Substances	Nitric Oxide (31C4KY9ESH) ; alpha-MSH (581-05-5) ; NOS2 protein, human (EC 1.14.13.39) ; NOS3 protein, human (EC 1.14.13.39) ; Nitric Oxide Synthase (EC 1.14.13.39) ; Nitric Oxide Synthase Type II (EC 1.14.13.39) ; Nitric Oxide Synthase Type III (EC 1.14.13.39)
Language	English
Publishing date	1998-05
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1151092-4
ISSN	1535-3842 ; 1062-4821 ; 1062-4813
ISSN (online)	1535-3842
ISSN	1062-4821 ; 1062-4813
DOI	10.1097/00041552-199805000-00009
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3686: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Stroma-free hemoglobin: a potential blood substitute.

Lieberthal, W

The Journal of laboratory and clinical medicine

1995 Volume 126, Issue 3, Page(s) 231–232

MeSH term(s)	Animals ; Blood Substitutes ; Hemoglobins/adverse effects ; Humans ; Rats
Chemical Substances	Blood Substitutes ; Hemoglobins ; hemoglobin, stroma free
Language	English
Publishing date	1995-09
Publishing country	United States
Document type	Comment ; Editorial
ZDB-ID	80208-6
ISSN	1532-6543 ; 0022-2143
ISSN (online)	1532-6543
ISSN	0022-2143
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ud II Zs.42: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito